ArticleJournal of bacteriology2013
Identification, purification, and characterization of a novel amino acid racemase, isoleucine 2-epimerase, from Lactobacillus species.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 56 citations in OpenAlex.
- Identification and characterization of RacX, a new broad-specificity amino acid racemase from a novel taxon within the orderApplied and environmental microbiology · 2026Article
- Exploring the Evolution-Coupling Hypothesis: Do Enzymes' Performance Gains Correlate with Increased Dissipation?Entropy (Basel, Switzerland) · 2025Article
- Identification and Characterization of a Novel d-Branched-Chain Amino Acids Importer from Lactobacillus fermentum.Chembiochem : a European journal of chemical biology · 2025Article
- Promising applications of D-amino acids in periprosthetic joint infection.Bone research · 2023Review
- Antihypertensive and Probiotic Effects of Hidakakombu (Foods (Basel, Switzerland) · 2021Article
- Small molecule natural products in human nasal/oral microbiota.Journal of industrial microbiology & biotechnology · 2021Review
- Identification and biochemical characterization of threonine dehydratase from the hyperthermophile Thermotoga maritima.Amino acids · 2021Article
- Article
- Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.Chemical Society reviews · 2021Review
- TK1211 Encodes an Amino Acid Racemase towards Leucine and Methionine in the Hyperthermophilic Archaeon Thermococcus kodakarensis.Journal of bacteriology · 2021Article
- Advances in D-Amino Acids in Neurological Research.International journal of molecular sciences · 2020Review
- d-Amino Acids and Lactic Acid Bacteria.Microorganisms · 2019Review
- Production of d-Branched-Chain Amino Acids by Lactic Acid Bacteria Carrying Homologs to Isoleucine 2-Epimerase ofFrontiers in microbiology · 2018Article
- A Novel PLP-Dependent Alanine/Serine Racemase From the Hyperthermophilic ArchaeonFrontiers in microbiology · 2018Article
- A Novel Bifunctional Amino Acid Racemase With Multiple Substrate Specificity, MalY FromFrontiers in microbiology · 2018Article
- Potent anti-seizure effects of D-leucine.Neurobiology of disease · 2015Article
- Discovery of a novel amino acid racemase through exploration of natural variation in Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Genetic determinants of reutericyclin biosynthesis in Lactobacillus reuteri.Applied and environmental microbiology · 2015Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Accumulation of d-leucine, d-allo-isoleucine, and d-valine was observed in the growth medium of a lactic acid bacterium, Lactobacillus otakiensis JCM 15040, and the racemase responsible was purified from the cells and identified. The N-terminal amino acid sequence of the purified enzyme was GKLDKASKLI, which is consistent with that of a putative γ-aminobutyrate aminotransferase from Lactobacillus buchneri. The putative γ-aminobutyrate aminotransferase gene from L. buchneri JCM 1115 was expressed in recombinant Escherichia coli and then purified to homogeneity. The enzyme catalyzed the racemization of a broad spectrum of nonpolar amino acids. In particular, it catalyzed at high rates the epimerization of l-isoleucine to d-allo-isoleucine and d-allo-isoleucine to l-isoleucine. In contrast, the enzyme showed no γ-aminobutyrate aminotransferase activity. The relative molecular masses of the subunit and native enzyme were estimated to be about 49 kDa and 200 kDa, respectively, indicating that the enzyme was composed of four subunits of equal molecular masses. The Km and Vmax values of the enzyme for l-isoleucine were 5.00 mM and 153 μmol·min(-1)·mg(-1), respectively, and those for d-allo-isoleucine were 13.2 mM and 286 μmol·min(-1)·mg(-1), respectively. Hydroxylamine and other inhibitors of pyridoxal 5'-phosphate-dependent enzymes completely blocked the enzyme activity, indicating the enzyme requires pyridoxal 5'-phosphate as a coenzyme. This is the first evidence of an amino acid racemase that specifically catalyzes racemization of nonpolar amino acids at the C-2 position.
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